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P03188 (GB_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Envelope glycoprotein B

Short name=gB
Alternative name(s):
GP115
Glycoprotein GP110
Gene names
Name:gB
ORF Names:BALF4
OrganismEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]
Taxonomic identifier10377 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Envelope glycoprotein that forms spikes at the surface of virion envelope. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding of gp350/220 to its receptor, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis By similarity.

Subunit structure

Homotrimer; disulfide-linked By similarity. Ref.6

Subcellular location

Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. Host endosome membrane; Single-pass type I membrane protein By similarity. Host Golgi apparatus membrane; Single-pass type I membrane protein By similarity. Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) By similarity. Ref.4

Post-translational modification

A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds Probable.

Sequence similarities

Belongs to the herpesviridae glycoprotein B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 857835Envelope glycoprotein B
PRO_0000038190

Regions

Topological domain23 – 732710Virion surface Potential
Transmembrane733 – 75321Helical; Potential
Topological domain754 – 857104Intravirion Potential
Region111 – 1144Involved in fusion and/or binding to host membrane Potential
Region193 – 1975Involved in fusion and/or binding to host membrane Potential
Region561 – 62060Oligomerization
Region709 – 72921Hydrophobic membrane proximal region
Compositional bias428 – 4325Poly-Arg
Compositional bias836 – 8394Poly-Arg

Sites

Site432 – 4332Cleavage; by host furin Potential

Amino acid modifications

Glycosylation761N-linked (GlcNAc...); by host Potential
Glycosylation1631N-linked (GlcNAc...); by host Ref.8
Glycosylation2901N-linked (GlcNAc...); by host Ref.8
Glycosylation3291N-linked (GlcNAc...); by host Potential
Glycosylation3481N-linked (GlcNAc...); by host Potential
Glycosylation3951N-linked (GlcNAc...); by host Potential
Glycosylation4361N-linked (GlcNAc...); by host Potential
Glycosylation5631N-linked (GlcNAc...); by host Potential
Glycosylation6291N-linked (GlcNAc...); by host Ref.8
Disulfide bond51 ↔ 528
Disulfide bond68 ↔ 484
Disulfide bond141 ↔ 206
Disulfide bond295 ↔ 342
Disulfide bond551 ↔ 588 By similarity

Experimental info

Mutagenesis112 – 1132WY → HR: Loss of fusion with epithelial cells.
Mutagenesis193 – 1964WLIW → RVEA: Loss of fusion with epithelial cells. Ref.5
Mutagenesis428 – 4325RRRRR → DDDDK: Complete loss of proteolytic cleavage. Ref.5

Secondary structure

................................................................................ 857
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03188 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: D9BCE9487D8A1411

FASTA85795,639
        10         20         30         40         50         60 
MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV CELSSHGDLF 

        70         80         90        100        110        120 
RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT KIVTNILIYN GWYADSVTNR 

       130        140        150        160        170        180 
HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD GLTRVYVDRD GVNITVNLKP TGGLANGVRR 

       190        200        210        220        230        240 
YASQTELYDA PGWLIWTYRT RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN 

       250        260        270        280        290        300 
KETFHERADS FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW 

       310        320        330        340        350        360 
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT MHEKYEAVQD 

       370        380        390        400        410        420 
RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT TPTSSPPSSP SPPAPSAARG 

       430        440        450        460        470        480 
STPAAVLRRR RRDAGNATTP VPPTAPGKSL GTLNNPATVQ IQFAYDSLRR QINRMLGDLA 

       490        500        510        520        530        540 
RAWCLEQKRQ NMVLRELTKI NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK 

       550        560        570        580        590        600 
SMRVPGSETM CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN 

       610        620        630        640        650        660 
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR ASNVFDLEGI 

       670        680        690        700        710        720 
FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL GSVGQSITNL VSTVGGLFSS 

       730        740        750        760        770        780 
LVSGFISFFK NPFGGMLILV LVAGVVILVI SLTRRTRQMS QQPVQMLYPG IDELAQQHAS 

       790        800        810        820        830        840 
GEGPGINPIS KTELQAIMLA LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY 

       850 
HDPETAAALL GEAETEF 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus."
Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.
Mol. Biol. Med. 1:21-45(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence and expression of the B95-8 Epstein-Barr virus genome."
Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G.
Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB."
Gong M., Ooka T., Matsuo T., Kieff E.
J. Virol. 61:499-508(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROTEIN.
[4]"Proteins of purified Epstein-Barr virus."
Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E., Illanes D., Sarracino D., Kieff E.
Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
[5]"Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins."
Backovic M., Leser G.P., Lamb R.A., Longnecker R., Jardetzky T.S.
Virology 368:102-113(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 112-TRP-TYR-113; 193-TRP--TRP-196 AND 428-ARG--ARG-432, PROTEOLYTIC CLEAVAGE.
[6]"Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis."
Reimer J.J., Backovic M., Deshpande C.G., Jardetzky T., Longnecker R.
J. Virol. 83:734-747(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: OLIGOMERIZATION REGION.
[7]"Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells."
Sorem J., Longnecker R.
J. Gen. Virol. 90:591-595(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC CLEAVAGE BY HOST FURIN.
[8]"Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B."
Backovic M., Longnecker R., Jardetzky T.S.
Proc. Natl. Acad. Sci. U.S.A. 106:2880-2885(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-685, GLYCOSYLATION AT ASN-163; ASN-290 AND ASN-629.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01555 Genomic DNA. Translation: CAA24806.1.
AJ507799 Genomic DNA. Translation: CAD53463.1.
PIRQQBE1L. A03749.
RefSeqYP_401713.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FVCX-ray3.20A23-685[»]
ProteinModelPortalP03188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47669N.
MINTMINT-6768112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3783680.

Phylogenomic databases

ProtClustDBPHA3231.

Family and domain databases

InterProIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamPF00606. Glycoprotein_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03188.

Entry information

Entry nameGB_EBVB9
AccessionPrimary (citable) accession number: P03188
Secondary accession number(s): Q777B0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references